A Subfamily of Dr Adhesins of Escherichia coli Bind Independently to Decay-accelerating Factor and the N-domain of Carcinoembryonic Antigen
| Autor: | Ernesto Cota, Alain L. Servin, Steve L. Moseley, Julie Guignot, Steve Matthews, Natalia Korotkova, Severine Monpouet, Yuri Lebedin |
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| Přispěvatelé: | Department of Microbiology, University of Washington [Seattle], THE DIVISION OF MOLECULAR BIOSCIENCES, Imperial College London, XEMA-MEDICA Co, Signalisation et physiopathologie des cellules épithéliales, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Codogno, Patrice |
| Rok vydání: | 2006 |
| Předmět: |
MESH: Adhesins
Bacterial MESH: Carcinoembryonic Antigen Fimbria MESH: Cricetinae CHO Cells Plasma protein binding Biology Biochemistry Article MESH: Cell Adhesion MESH: Fimbriae Bacterial MESH: Protein Structure Tertiary 03 medical and health sciences MESH: CHO Cells [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases Cricetinae Cell Adhesion Escherichia coli Animals Humans MESH: Protein Binding MESH: Animals Binding site Adhesins Bacterial Cell adhesion Receptor [SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology Molecular Biology Decay-accelerating factor 030304 developmental biology 0303 health sciences MESH: Humans CD55 Antigens MESH: Escherichia coli 030306 microbiology Cell adhesion molecule Cell Biology MESH: Antigens CD55 Molecular biology Carcinoembryonic Antigen Protein Structure Tertiary Bacterial adhesin [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Fimbriae Bacterial [SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases Protein Binding |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 281 (39), pp.29120-30. ⟨10.1074/jbc.M605681200⟩ |
| ISSN: | 0021-9258 1083-351X |
| Popis: | International audience; Escherichia coli expressing the Dr family of adhesins adheres to epithelial cells by binding to decay-accelerating factor (DAF) and carcinoembryonic antigen (CEA)-related cell surface proteins. The attachment of bacteria expressing Dr adhesins to DAF induces clustering of DAF around bacterial cells and also recruitment of CEA-related cell adhesion molecules. CEA, CEACAM1, and CEACAM6 have been shown to serve as receptors for some Dr adhesins (AfaE-I, AfaE-III, DraE, and DaaE). We demonstrate that AfaE-I, AfaE-V, DraE, and DaaE adhesins bind to the N-domain of CEA. To identify the residues involved in the N-CEA/DraE interaction, we performed SPR binding analyses of naturally occurring variants and a number of randomly generated mutants in DraE and N-CEA. Additionally, we used chemical shift mapping by NMR to determine the surface of DraE involved in N-CEA binding. These results show a distinct CEA binding site located primarily in the A, B, E, and D strands of the Dr adhesin. Interestingly, this site is located opposite to the beta-sheet encompassing the previously determined binding site for DAF, which implies that the adhesin can bind simultaneously to both receptors on the epithelial cell surface. The recognition of CEACAMs from a highly diverse DrCEA subfamily of Dr adhesins indicates that interaction with these receptors plays an important role in niche adaptation of E. coli strains expressing Dr adhesins. |
| Databáze: | OpenAIRE |
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